pone.0218507.g003.tif (1.54 MB)
Both original bNK2A-C10C20 and an analog bNK2A-S10S20 peptides displayed strong antimicrobial activities against Histophilus somni.
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posted on 2019-06-19, 17:37 authored by Rohana P. Dassanayake, Shollie M. Falkenberg, Eric M. Nicholson, Robert E. Briggs, Fred M. Tatum, Vijay K. Sharma, Timothy A. Reinhardt(A). Two bovine H. somni pneumonic isolates (91 and 2336) were incubated with indicated concentrations of peptides or PBS (control) and incubated at 37°C in a humidified atmosphere of 7.5% CO2 for 60 min. (B). The original bNK2A-C10C20 peptide (20 μM) was pre-incubated with 0.2, 0.5, and 1.0 mM DTT for 20 min before incubation with H. somni (91 and 2336). Results shown are the means and SD of three independent experiments.
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well-conserved cysteine residuesbNK 2A antimicrobial activity30- mer bNK 2A peptidesintra-chain disulfide bondsbNK 2A peptideMature NK-lysin proteinbactericidal activity Bovine NK-lysinsdisulfide bondsbNK 2A forms disulfide bondsα- helical structuresNK-lysin-derived peptides show antimicrobial activityNK-lysin-derived peptidecationic antimicrobial proteins
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